The NG GTPase domain of Ffh, the bacterial homolog of the signal sequence recognition protein SRP54, reveals several unique features that should contribute to our understanding of GTPase structure-function in general. Crystals of the apo-form of the domain diffract to beyond 1.0 E resolution at a synchrotron X-ray source (SSRL BL 7-1), and crystals of the GDP-bound domain diffract almost as well. During previous work we have developed methods for efficient data collection from these crystals to that resolution. Our efforts are now directed at obtaining complete well measured data to ultra-high resolution from both crystal forms.